6ZIB

CRYSTAL STRUCTURE OF RAT PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE-1 (RPMFE1) COMPLEXED WITH ACETOACETYL-COA AND NADH

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
AAA	0003824	molecular_function	catalytic activity
AAA	0003857	molecular_function	3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
AAA	0004165	molecular_function	delta(3)-delta(2)-enoyl-CoA isomerase activity
AAA	0004300	molecular_function	enoyl-CoA hydratase activity
AAA	0005777	cellular_component	peroxisome
AAA	0005782	cellular_component	peroxisomal matrix
AAA	0005829	cellular_component	cytosol
AAA	0006629	biological_process	lipid metabolic process
AAA	0006631	biological_process	fatty acid metabolic process
AAA	0006635	biological_process	fatty acid beta-oxidation
AAA	0006636	biological_process	unsaturated fatty acid biosynthetic process
AAA	0016491	molecular_function	oxidoreductase activity
AAA	0016509	molecular_function	long-chain-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
AAA	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
AAA	0016829	molecular_function	lyase activity
AAA	0016853	molecular_function	isomerase activity
AAA	0016863	molecular_function	intramolecular oxidoreductase activity, transposing C=C bonds
AAA	0018812	molecular_function	3-hydroxyacyl-CoA dehydratase activity
AAA	0019899	molecular_function	enzyme binding
AAA	0033540	biological_process	fatty acid beta-oxidation using acyl-CoA oxidase
AAA	0036109	biological_process	alpha-linolenic acid metabolic process
AAA	0042759	biological_process	long-chain fatty acid biosynthetic process
AAA	0070403	molecular_function	NAD+ binding
AAA	1901570	biological_process	fatty acid derivative biosynthetic process
BBB	0003824	molecular_function	catalytic activity
BBB	0003857	molecular_function	3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
BBB	0004165	molecular_function	delta(3)-delta(2)-enoyl-CoA isomerase activity
BBB	0004300	molecular_function	enoyl-CoA hydratase activity
BBB	0005777	cellular_component	peroxisome
BBB	0005782	cellular_component	peroxisomal matrix
BBB	0005829	cellular_component	cytosol
BBB	0006629	biological_process	lipid metabolic process
BBB	0006631	biological_process	fatty acid metabolic process
BBB	0006635	biological_process	fatty acid beta-oxidation
BBB	0006636	biological_process	unsaturated fatty acid biosynthetic process
BBB	0016491	molecular_function	oxidoreductase activity
BBB	0016509	molecular_function	long-chain-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
BBB	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
BBB	0016829	molecular_function	lyase activity
BBB	0016853	molecular_function	isomerase activity
BBB	0016863	molecular_function	intramolecular oxidoreductase activity, transposing C=C bonds
BBB	0018812	molecular_function	3-hydroxyacyl-CoA dehydratase activity
BBB	0019899	molecular_function	enzyme binding
BBB	0033540	biological_process	fatty acid beta-oxidation using acyl-CoA oxidase
BBB	0036109	biological_process	alpha-linolenic acid metabolic process
BBB	0042759	biological_process	long-chain fatty acid biosynthetic process
BBB	0070403	molecular_function	NAD+ binding
BBB	1901570	biological_process	fatty acid derivative biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00067
Number of Residues	25
Details	3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. NcyGFVgNRmlaPYYnqgff.LLeeG

Chain	Residue	Details
AAA	ASN474-GLY498

---

site_id	PS00166
Number of Residues	21
Details	ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. LAaIQGvalGGGlelaLgCHY

Chain	Residue	Details
AAA	LEU90-TYR110

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
AAA	GLY100
BBB	GLY100

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	SITE: Important for catalytic activity => ECO:0000250

Chain	Residue	Details
AAA	GLU103
AAA	GLU123
BBB	GLU103
BBB	GLU123

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Blocked amino end (Ala)

Chain	Residue	Details
AAA	ALA2
BBB	ALA2

---

site_id	SWS_FT_FI4
Number of Residues	20
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9DBM2

Chain	Residue	Details
AAA	LYS38
AAA	LYS721
BBB	LYS38
BBB	LYS182
BBB	LYS241
BBB	LYS253
BBB	LYS279
BBB	LYS289
BBB	LYS330
BBB	LYS531
BBB	LYS576
AAA	LYS182
BBB	LYS721
AAA	LYS241
AAA	LYS253
AAA	LYS279
AAA	LYS289
AAA	LYS330
AAA	LYS531
AAA	LYS576

---

site_id	SWS_FT_FI5
Number of Residues	14
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DBM2

Chain	Residue	Details
AAA	LYS173
BBB	LYS218
BBB	LYS275
BBB	LYS583
BBB	LYS590
BBB	LYS709
AAA	LYS190
AAA	LYS218
AAA	LYS275
AAA	LYS583
AAA	LYS590
AAA	LYS709
BBB	LYS173
BBB	LYS190

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DBM2

Chain	Residue	Details
AAA	LYS249
AAA	LYS359
AAA	LYS463
BBB	LYS249
BBB	LYS359
BBB	LYS463

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q08426

Chain	Residue	Details
AAA	LYS345
BBB	LYS345

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q08426

Chain	Residue	Details
AAA	THR547
BBB	THR547

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